Lathe R, Lecocq J P
Mol Gen Genet. 1977 Jul 7;154(1):53-60. doi: 10.1007/BF00265576.
The firA gene probably codes for an essential component of the transcription machinery in E. coli. Bacterial proteins coded by lambdafirA transducing phages have been examined after infection of a UV-irradiated lambda lysogen, and 2 major fir-specific proteins have been characterized. The larger protein has a molecular weight of 27,000 daltons. The smaller protein, of 17,000 daltons, is produced in a considerable molar excess over the larger protein, is basic and binds strongly to DNA-, to DEAE- and to phospho-cellulose. This protein is clearly visible upon 2-dimensional gel electrophoresis of unfractionated E. coli protein, showing that it is present in the cell in large quantities. Evidence is presented to suggest that this protein may be identical to the Kappa factor of Schäfer and Zillig (1973).
firA基因可能编码大肠杆菌转录机制中的一个必需成分。在用紫外线照射过的λ溶原菌感染后,对由λfirA转导噬菌体编码的细菌蛋白进行了检测,已鉴定出2种主要的fir特异性蛋白。较大的蛋白分子量为27,000道尔顿。较小的蛋白分子量为17,000道尔顿,其摩尔产量大大超过较大的蛋白,呈碱性,并且与DNA、二乙氨基乙基纤维素和磷酸纤维素强烈结合。在未分级的大肠杆菌蛋白的二维凝胶电泳中可以清楚地看到这种蛋白,表明它在细胞中大量存在。有证据表明,这种蛋白可能与舍费尔和齐利格(1973年)发现的κ因子相同。